Alpha-Keto Acid Dehydrogenase Complexes
Found in all organisms, the alpha-keto acid dehydrogenase complexes have central roles in cellular metabolism and are major sites of regulation. The understanding of the organization, function and regulation of these quintessential multienzyme complexes has been greatly advanced by studies employing...
| Other Authors: | , , |
|---|---|
| Format: | eBook |
| Language: | English |
| Published: |
Basel
Birkhäuser
1996, 1996
|
| Edition: | 1st ed. 1996 |
| Series: | Molecular and Cell Biology Updates
|
| Subjects: | |
| Online Access: | |
| Collection: | Springer Book Archives -2004 - Collection details see MPG.ReNa |
Table of Contents:
- Interaction of protein domains in the assembly and mechanism of 2-oxo acid dehydrogenase multienzyme complexes
- Probing the active site of mammalian pyruvate dehydrogenase
- Role of the E2 core in the dominant mechanisms of regulatory control of mammalian pyruvate dehydrogenase complex
- Lipoamide dehydrogenase
- Plant pyruvate dehydrogenase complexes
- Regulation of the pyruvate dehydrogenase complex during the aerobic/anaerobic transition in the development of the parasitic nematode, Ascaris suum
- Structure, function and assembly of mammalian branched-chain ?-ketoacid dehydrogenase complex
- Lipoylation of E2 component
- Pyruvate dehydrogenase phosphatase
- The mitochondrial ?-ketoacid dehydrogenase kinases: Molecular cloning, tissue-specific expression and primary structure analysis
- Shorter term and longer term regulation of pyruvate dehydrogenase kinases
- Hormonal and nutritional modulation of PDHC activity status
- Regulation of branched-chain ?-keto acid dehydrogenase complex in rat liver and skeletal muscle by exercise and nutrition
- Dephosphorylation of PDH by phosphoprotein phosphatases and its allosteric regulation by inositol glycans
- Long-term regulation and promoter analysis of mammalian pyruvate dehydrogenase complex
- The sperm-specific pyruvate dehydrogenase E1? genes
- Molecular defects of the branched-chain ?-keto acid dehydrogenase complex: maple syrup urine disease due to mutations of the E1? or E1? subunit gene
- Human defects of the pyruvate dehydrogenase complex
- Multigenic basis for maple syrup urine disease with emphasis on mutations in branched chain dihydrolipoyl acyltransferase
- Structure and chromosomal localization of the human 2-oxoglutarate dehydrogenase gene
- Pyruvate dehydrogenase complex as an autoantigen in primarybiliary cirrhosis